ArticleRSC advances2020
Inhibitory effect of coumarin and its analogs on insulin fibrillation /cytotoxicity is depend on oligomerization states of the protein.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- The effect of novel antihypertensive drug valsartan on lysozyme aggregation: A combined in situ and in silico study.Heliyon · 2023Article
- Coumarin derivatives inhibit the aggregation of β-lactoglobulin.RSC advances · 2022Article
- The inhibitory effect of curcumin loaded poly (vinyl caprolactam) nanohydrogel on insulin fibrillation.Process biochemistry (Barking, London, England) · 2022Article
- Oligomeric procyanidins inhibit insulin fibrillation by forming unstructured and off-pathway aggregates.RSC advances · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Looking through a historical lens, attention to the stabilization of pharmaceutical proteins/peptides has been dramatically increased. Human insulin is the most challenging and the most widely used pharmaceutical protein in the world. In this study, the protein and coumarin as a plant-derived phenolic compound and two coumarin analogs with different moieties were investigated to evaluate the protein fibrillation and cytotoxicity. The obtained data showed that with a change in environmental pH, the behavior of the compounds on the process of insulin fibrillation will be changed completely. Coumarin (C1) and its hydrophobic analog, 7-methyl coumarin (C2), in an acidic environment, inhibit insulin fibrillation, change the oligomerization state of insulin and produce fibrils with notable lateral interactions with low cytotoxicity. However, negatively-charged 3-trifluoromethyl coumarin (C3) without significant changes in insulin structure and by altering the oligomerization state of the protein, slightly accelerates hormone fibrillation. Also, the compounds showed a disulfide protecting role during protein aggregation. Regarding the toxicity of the fibrils, it was observed that in addition to the secondary structures of proteinous fibrils, the ability to destroy the cell membrane is also related to the length of the fibrils and their degree of lateral interactions. By and large, this work can be useful in finding a better formulation for bio-pharmaceutical macro-molecules.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.